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Literature summary for 1.8.98.1 extracted from

  • Fielding, A.J.; Parey, K.; Ermler, U.; Scheller, S.; Jaun, B.; Bennati, M.
    Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate: quinone reductase (2013), J. Biol. Inorg. Chem., 18, 905-915.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Iron-sulfur cluster the cluster is fixed by cysteines of two cysteine-rich CCG domain sequence motifs (CX31-39CCX35-36CXXC) of subunit HdrB of the Methanothermobacter marburgensis HdrABC complex. An Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain is performed Methanothermobacter marburgensis

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
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-
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Methanothermobacter marburgensis Q50755 subunit HdrB
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Methanothermobacter marburgensis DSM 2133 Q50755 subunit HdrB
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Synonyms

Synonyms Comment Organism
heterodisulfide reductase
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Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
Fe-S center subunit HdrB contains a Fe-S cluster fixed by cysteines of two cysteine-rich CCG domain sequence motifs, CX31-39CCX35-36CXXC. Electron paramagnetic resonance spectra are consistent with with the attachment of the substrate to the cluster in HdrABC and infer that the cluster's magnetic properties arise from the CCG binding motif Methanothermobacter marburgensis